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Protein

Uridylate kinase

Gene

SPCC1795.05c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.UniRule annotation

Catalytic activityi

ATP + UMP = ADP + UDP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39NMPUniRule annotation1
Binding sitei98NMPUniRule annotation1
Binding sitei129ATPUniRule annotation1
Binding sitei135NMPUniRule annotation1
Binding sitei146NMPUniRule annotation1
Binding sitei174ATP; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 17ATPUniRule annotation6
Nucleotide bindingi61 – 63NMPUniRule annotation3
Nucleotide bindingi91 – 94NMPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-499943 Interconversion of nucleotide di- and triphosphates

Names & Taxonomyi

Protein namesi
Recommended name:
Uridylate kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
Short name:
UKUniRule annotation
Alternative name(s):
ATP:UMP phosphotransferaseUniRule annotation
Deoxycytidylate kinaseUniRule annotation
Short name:
CKUniRule annotation
Short name:
dCMP kinaseUniRule annotation
Uridine monophosphate kinaseUniRule annotation
Short name:
UMP kinaseUniRule annotation
Short name:
UMPKUniRule annotation
Gene namesi
ORF Names:SPCC1795.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.05c
PomBaseiSPCC1795.05c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589461 – 191Uridylate kinaseAdd BLAST191

Proteomic databases

MaxQBiO59771
PaxDbiO59771
PRIDEiO59771

PTM databases

iPTMnetiO59771

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi275517, 1 interactor
STRINGi4896.SPCC1795.05c.1

Structurei

3D structure databases

ProteinModelPortaliO59771
SMRiO59771
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 63NMPbindUniRule annotationAdd BLAST31
Regioni128 – 138LIDUniRule annotationAdd BLAST11

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000238771
InParanoidiO59771
KOiK13800
OMAiFCHLSAG
OrthoDBiEOG092C5OQU
PhylomeDBiO59771

Family and domain databases

CDDicd01428 ADK, 1 hit
HAMAPiMF_00235 Adenylate_kinase_Adk, 1 hit
MF_03172 Adenylate_kinase_UMP_CMP_kin, 1 hit
InterProiView protein in InterPro
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR027417 P-loop_NTPase
IPR006266 UMP_CMP_kinase
PANTHERiPTHR23359 PTHR23359, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01359 UMP_CMP_kin_fam, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 1 hit

Sequencei

Sequence statusi: Complete.

O59771-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYNVIFVLGG PGAGKGTQCD RLAEKFDKFV HISAGDCLRE EQNRPGSKYG
60 70 80 90 100
NLIKEYIKDG KIVPMEITIS LLETKMKECH DKGIDKFLID GFPREMDQCE
110 120 130 140 150
GFEKSVCPAK FALYFRCGQE TMLKRLIHRG KTSGRSDDNI ESIKKRFVTY
160 170 180 190
TKASMPVVEY LKSQNRLITI DAEQDPDAVF EDTVKALQPY L
Length:191
Mass (Da):21,716
Last modified:August 1, 1998 - v1
Checksum:iAD344378AC334757
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA Translation: CAA18640.1
PIRiT41138
RefSeqiNP_588039.1, NM_001023031.2

Genome annotation databases

EnsemblFungiiSPCC1795.05c.1; SPCC1795.05c.1:pep; SPCC1795.05c
KEGGispo:SPCC1795.05c

Similar proteinsi

Entry informationi

Entry nameiKCY_SCHPO
AccessioniPrimary (citable) accession number: O59771
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: August 1, 1998
Last modified: March 28, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health